Structural basis of staphylococcal Stl inhibition on a eukaryotic dUTPase
文献类型：期刊论文
| 作者 | Wang, Fang1,2,3; Liu, Changshui1,2,4; Wang, Chongyang1,2,3; Wang, Yan1,2,3; Zang, Kun1,2,3; Wang, Xin1,2,3; Liu, Xiaohua5; Li, Shihao1,2,3,4; Li, Fuhua1,2,3,4; Ma, Qingjun1,2,3,4 |
| 刊名 | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
 |
| 出版日期 | 2021-08-01 |
| 卷号 | 184页码:821-830 |
| 关键词 | Stl dUTPase interactions Proteinaceous inhibitor Crystal structure |
| ISSN号 | 0141-8130 |
| DOI | 10.1016/j.ijbiomac.2021.06.107 |
| 通讯作者 | Ma, Qingjun(qma@qdio.ac.cn) |
| 英文摘要 | dUTPases are key enzymes in all life kingdoms. A staphylococcal repressor protein (Stl) inhibited dUTPases from multiple species to various extents. Understanding the molecular basis underlying the inhibition differences is crucial to develop effective proteinaceous inhibitors of dUTPases. Herein, we report the complex structure of Stl N-terminal domain (StlN-ter) and Litopenaeus vannamei dUTPase domain (lvDUT65-210). Stl inhibited lvDUT65-210 through its N-terminal domain. The lvDUT65-210-StlN-ter complex structure revealed a heterohexamer encompassing three StlN-ter monomers bound to one lvDUT65-210 trimer, generating two types of Stl-dUTPase interfaces. Interface I is formed by Stl interaction with the lvDUT65-210 active-site region that is contributed by motifs I-IV from its two subunits; interface II results from Stl binding to the C-terminal motif V of the third lvDUT65-210 subunit. Structural comparison revealed both conserved features and obvious differences in Stl-dUTPase interaction patterns, giving clues about the inhibition differences of Stl on dUTPases. Noticeably, interface II is only observed in lvDUT65-210-StlN-ter. The Stl-interacting residues of lvDUT65-210 are conserved in other eukaryotic dUTPases, particularly human dUTPase. Altogether, our study presents the first structural model of Stl interaction with eukaryotic dUTPase, contributing to a more complete view of Stl inhibition and facilitating the development of proteinaceous inhibitor for eukaryotic dUTPases. |
| 资助项目 | National Natural Science Foundation of China[31572660] ; National Natural Science Foundation of China[31872600] ; Qingdao Innovation Leadership Program[18-1-2-12-zhc] ; Laboratory for Marine Biology and Biotechnology, Qingdao Pilot National Laboratory for Marine Science and Technology[OF2015NO12] |
| WOS研究方向 | Biochemistry & Molecular Biology ; Chemistry ; Polymer Science |
| 语种 | 英语 |
| WOS记录号 | WOS:000684600700007 |
| 出版者 | ELSEVIER |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/176007]  |
| 专题 | 海洋研究所_实验海洋生物学重点实验室 |
| 通讯作者 | Ma, Qingjun |
| 作者单位 | 1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Nanhai Rd 7, Qingdao 266071, Peoples R China 2.Pilot Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao, Peoples R China 3.Univ Chinese Acad Sci, Beijing, Peoples R China 4.Chinese Acad Sci, Ctr Ocean Megasci, Qingdao, Peoples R China 5.Ocean Univ China, Coll Marine Life Sci, Qingdao, Peoples R China |
| 推荐引用方式 GB/T 7714 | Wang, Fang,Liu, Changshui,Wang, Chongyang,et al. Structural basis of staphylococcal Stl inhibition on a eukaryotic dUTPase[J]. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,2021,184:821-830. |
| APA | Wang, Fang.,Liu, Changshui.,Wang, Chongyang.,Wang, Yan.,Zang, Kun.,...&Ma, Qingjun.(2021).Structural basis of staphylococcal Stl inhibition on a eukaryotic dUTPase.INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,184,821-830. |
| MLA | Wang, Fang,et al."Structural basis of staphylococcal Stl inhibition on a eukaryotic dUTPase".INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 184(2021):821-830. |
入库方式： OAI收割
来源：海洋研究所
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